4dm7: Difference between revisions
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==Crystal structure of the CFTR inhibitory factor Cif with the E153D mutation== | ==Crystal structure of the CFTR inhibitory factor Cif with the E153D mutation== | ||
<StructureSection load='4dm7' size='340' side='right' caption='[[4dm7]], [[Resolution|resolution]] 1.36Å' scene=''> | <StructureSection load='4dm7' size='340' side='right'caption='[[4dm7]], [[Resolution|resolution]] 1.36Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4dm7]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4dm7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_UCBPP-PA14 Pseudomonas aeruginosa UCBPP-PA14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DM7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DM7 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.36Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dm7 OCA], [https://pdbe.org/4dm7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dm7 RCSB], [https://www.ebi.ac.uk/pdbsum/4dm7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dm7 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0H2ZD27_PSEAB A0A0H2ZD27_PSEAB] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 17: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 4dm7" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4dm7" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[CFTR inhibitory factor|CFTR inhibitory factor]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pseudomonas aeruginosa UCBPP-PA14]] | ||
[[Category: | [[Category: Bahl CD]] | ||
[[Category: | [[Category: Madden DR]] | ||
Latest revision as of 09:27, 17 October 2024
Crystal structure of the CFTR inhibitory factor Cif with the E153D mutationCrystal structure of the CFTR inhibitory factor Cif with the E153D mutation
Structural highlights
FunctionPublication Abstract from PubMedOpportunistic pathogens exploit diverse strategies to sabotage host defenses. Pseudomonas aeruginosa secretes the CFTR inhibitory factor Cif and thus triggers loss of CFTR, an ion channel required for airway mucociliary defense. However, the mechanism of action of Cif has remained unclear. It catalyzes epoxide hydrolysis, but there is no known role for natural epoxides in CFTR regulation. It was demonstrated that the hydrolase activity of Cif is strictly required for its effects on CFTR. A small-molecule inhibitor that protects this key component of the mucociliary defense system was also uncovered. These results provide a basis for targeting the distinctive virulence chemistry of Cif and suggest an unanticipated role of physiological epoxides in intracellular protein trafficking. Inhibiting an epoxide hydrolase virulence factor from Pseudomonas aeruginosa protects CFTR.,Bahl CD, Hvorecny KL, Bomberger JM, Stanton BA, Hammock BD, Morisseau C, Madden DR Angew Chem Int Ed Engl. 2015 Jul 1. doi: 10.1002/anie.201503983. PMID:26136396[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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